ID A0A159Z4H0_9RHOB Unreviewed; 426 AA.
AC A0A159Z4H0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=O-acetylhomoserine aminocarboxypropyltransferase/O-acetylserine sulfhydrylase {ECO:0000313|EMBL:AMY70092.1};
GN ORFNames=AKL17_2856 {ECO:0000313|EMBL:AMY70092.1};
OS Frigidibacter mobilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Frigidibacter.
OX NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY70092.1, ECO:0000313|Proteomes:UP000076128};
RN [1] {ECO:0000313|EMBL:AMY70092.1, ECO:0000313|Proteomes:UP000076128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA Geng S., Pan X., Wu X.;
RT "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT oilfield in Xinjiang.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR EMBL; CP012661; AMY70092.1; -; Genomic_DNA.
DR RefSeq; WP_066814197.1; NZ_CP012661.1.
DR AlphaFoldDB; A0A159Z4H0; -.
DR STRING; 1335048.AKL17_2856; -.
DR KEGG; daa:AKL17_2856; -.
DR PATRIC; fig|1335048.3.peg.2969; -.
DR OrthoDB; 9805807at2; -.
DR Proteomes; UP000076128; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Transferase {ECO:0000313|EMBL:AMY70092.1}.
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 426 AA; 45043 MW; 3C95B13FDA760E9D CRC64;
MTQGFDTLQV HAGTAPDPAT GARQVPIYQT TAYVFRDADH AARLFGLQEV GYIYSRLTNP
TVSALANRIA ALEGGVGAVC CSSGHAAQIM ALFPLMGPGL NIVASTRLYG GTITQFSQTF
KRFGWSARFV DFDDEAAVAA AIDDDTRAVF CESISNPGGY VTDLPAIAAI ADKAGIPLIV
DNTLASPYLC RPIEHGATLV VHSTTKYLTG NGTVTGGAIV DAGTFDWSAS GKFPSLSAPE
PAYHGLKFHE ALGGMAFTFH SIAIGLRDLG MTMNPQAAHY TLMGIETLSL RMEKHVANAK
AVAEWLEKDP RVEFVTYAGL ASSPWNARVE RICPKGAGAL FTFAVKGGYE ACVKLVDALQ
LFSHVANLGD TRSLVIHSAS TTHRQLTPEQ QQAAGAAPNV VRLSIGIENV EDLIADLDQA
LAVATA
//
